GSP_CRIFA
ID GSP_CRIFA Reviewed; 719 AA.
AC P90518;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Glutathionylspermidine synthase;
DE EC=6.3.1.8;
GN Name=GSP;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=HS6;
RX PubMed=9677355; DOI=10.1074/jbc.273.31.19383;
RA Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H.;
RT "Cloning and characterization of the two enzymes responsible for
RT trypanothione biosynthesis in Crithidia fasciculata.";
RL J. Biol. Chem. 273:19383-19390(1998).
RN [2]
RP PROTEIN SEQUENCE OF 191-209; 351-358; 512-530; 532-538 AND 695-710, AND
RP CHARACTERIZATION.
RX PubMed=1304372; DOI=10.1002/pro.5560010705;
RA Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H.;
RT "Purification of glutathionylspermidine and trypanothione synthetases from
RT Crithidia fasciculata.";
RL Protein Sci. 1:874-883(1992).
CC -!- FUNCTION: Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to
CC form glutathionylspermidine in the biosynthesis trypanothione
CC (N(1),N(8)-bis(glutathionyl)spermidine), which is involved in
CC maintaining intracellular thiol redox and in defense against oxidants.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione + spermidine = ADP + glutathionylspermidine
CC + H(+) + phosphate; Xref=Rhea:RHEA:21272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:57835, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; EC=6.3.1.8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glutathionylspermidine synthase preATP-grasp family. {ECO:0000305}.
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DR EMBL; U66520; AAC48361.2; -; Genomic_DNA.
DR AlphaFoldDB; P90518; -.
DR SMR; P90518; -.
DR BindingDB; P90518; -.
DR ChEMBL; CHEMBL3354; -.
DR KEGG; ag:AAC48361; -.
DR VEuPathDB; TriTrypDB:CFAC1_230008300; -.
DR BRENDA; 6.3.1.8; 1365.
DR SABIO-RK; P90518; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008885; F:glutathionylspermidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF03738; GSP_synth; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50911; CHAP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..719
FT /note="Glutathionylspermidine synthase"
FT /id="PRO_0000070442"
FT DOMAIN 54..200
FT /note="Peptidase C51"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT BINDING 350..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 689..691
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 350
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 719 AA; 80322 MW; 46069BE9C40EEEFC CRC64;
MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI TAACLPLSSF
ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT AEEVWREENL FVDVRDGRPV
EVVRTPNKST GPAPAVADIV VWGEGPETPF GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV
PFSREIAMRT TESGEVELLD EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF
PKHVDVPWLN TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS
SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR FDFGYDGKNV
VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG AKCVTYFQRL LTNEKVCPQH
RLIHFMIDED DEERYTARCM MGFAEQAGFR TKLCVKLVNF RYRDGPPSNA APLATPCDHP
TIVDGEDEEV LMVWKTWSWD TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV
TGSKAILPFM HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE
LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL VYQQRLFLKK
FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA RVVRDNVPLG VSYSDEGET
